1eeh

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[[Image:1eeh.gif|left|200px]]
[[Image:1eeh.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 1eeh |SIZE=350|CAPTION= <scene name='initialview01'>1eeh</scene>, resolution 1.9&Aring;
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The line below this paragraph, containing "STRUCTURE_1eeh", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=UMA:URIDINE-5&#39;-DIPHOSPHATE-N-ACETYLMURAMOYL-L-ALANINE'>UMA</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/UDP-N-acetylmuramoyl-L-alanine--D-glutamate_ligase UDP-N-acetylmuramoyl-L-alanine--D-glutamate ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.2.9 6.3.2.9] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE=
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-->
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|DOMAIN=
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{{STRUCTURE_1eeh| PDB=1eeh | SCENE= }}
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|RELATEDENTRY=[[1uag|1UAG]], [[2uag|2UAG]], [[3uag|3UAG]], [[4uag|4UAG]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1eeh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1eeh OCA], [http://www.ebi.ac.uk/pdbsum/1eeh PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1eeh RCSB]</span>
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}}
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'''UDP-N-ACETYLMURAMOYL-L-ALANINE:D-GLUTAMATE LIGASE'''
'''UDP-N-ACETYLMURAMOYL-L-ALANINE:D-GLUTAMATE LIGASE'''
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[[Category: Heijenoort, J van.]]
[[Category: Heijenoort, J van.]]
[[Category: Martin, L.]]
[[Category: Martin, L.]]
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[[Category: adp-forming enzyme]]
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[[Category: Adp-forming enzyme]]
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[[Category: ligase]]
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[[Category: Ligase]]
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[[Category: murd]]
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[[Category: Murd]]
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[[Category: peptidoglycan synthesis]]
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[[Category: Peptidoglycan synthesis]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 14:59:45 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:00:57 2008''
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Revision as of 11:59, 2 May 2008

Template:STRUCTURE 1eeh

UDP-N-ACETYLMURAMOYL-L-ALANINE:D-GLUTAMATE LIGASE


Overview

UDP-N-acetylmuramoyl-l-alanine:d-glutamate (MurD) ligase catalyses the addition of d-glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-l-alanine (UMA). The crystal structures of Escherichia coli in the substrate-free form and MurD complexed with UMA have been determined at 2.4 A and 1.88 A resolution, respectively. The MurD structure comprises three domains each of a topology reminiscent of nucleotide-binding folds. In the two structures the C-terminal domain undergoes a large rigid-body rotation away from the N-terminal and central domains. These two "open" structures were compared with the four published "closed" structures of MurD. In addition the comparison reveals which regions are affected by the binding of UMA, ATP and d-Glu. Also we compare and discuss two structurally characterized enzymes which belong to the same ligase superfamily: MurD and folylpolyglutamate synthetase (FGS). The analysis allows the identification of key residues involved in the reaction mechanism of FGS. The determination of the two "open" conformation structures represents a new step towards the complete elucidation of the enzymatic mechanism of the MurD ligase.

About this Structure

1EEH is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

"Open" structures of MurD: domain movements and structural similarities with folylpolyglutamate synthetase., Bertrand JA, Fanchon E, Martin L, Chantalat L, Auger G, Blanot D, van Heijenoort J, Dideberg O, J Mol Biol. 2000 Sep 1;301(5):1257-66. PMID:10966819 Page seeded by OCA on Fri May 2 14:59:45 2008

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